1hi8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hi8.gif|left|200px]]<br /><applet load="1hi8" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1hi8.gif|left|200px]]
-
caption="1hi8, resolution 2.5&Aring;" />
+
 
-
'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6'''<br />
+
{{Structure
 +
|PDB= 1hi8 |SIZE=350|CAPTION= <scene name='initialview01'>1hi8</scene>, resolution 2.5&Aring;
 +
|SITE= <scene name='pdbsite=CA1:The+Three+Conserved+Active+Site+Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The+Three+Conserved+Active+Site+Aspartate'>CA2</scene>, <scene name='pdbsite=MG1:Mg+Binding+Site+For+Chain+A'>MG1</scene> and <scene name='pdbsite=MG2:Mg+Binding+Site+For+Chain+B'>MG2</scene>
 +
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1HI8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=CA1:The+Three+Conserved+Active+Site+Aspartate'>CA1</scene>, <scene name='pdbsite=CA2:The+Three+Conserved+Active+Site+Aspartate'>CA2</scene>, <scene name='pdbsite=MG1:Mg+Binding+Site+For+Chain+A'>MG1</scene> and <scene name='pdbsite=MG2:Mg+Binding+Site+For+Chain+B'>MG2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI8 OCA].
+
1HI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI8 OCA].
==Reference==
==Reference==
-
A mechanism for initiating RNA-dependent RNA polymerization., Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI, Nature. 2001 Mar 8;410(6825):235-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11242087 11242087]
+
A mechanism for initiating RNA-dependent RNA polymerization., Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI, Nature. 2001 Mar 8;410(6825):235-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11242087 11242087]
[[Category: Bacteriophage phi-6]]
[[Category: Bacteriophage phi-6]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 22: Line 31:
[[Category: viral polymerase]]
[[Category: viral polymerase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:29 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:22 2008''

Revision as of 09:37, 20 March 2008


PDB ID 1hi8

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites: , , and
Ligands:
Coordinates: save as pdb, mmCIF, xml



RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6


Overview

In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail. Here we show that the 2 A resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage straight phi6 is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription.

About this Structure

1HI8 is a Single protein structure of sequence from Bacteriophage phi-6. Full crystallographic information is available from OCA.

Reference

A mechanism for initiating RNA-dependent RNA polymerization., Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI, Nature. 2001 Mar 8;410(6825):235-40. PMID:11242087

Page seeded by OCA on Thu Mar 20 11:37:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools